Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification

doi:10.1002/jcb.25051

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	Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification
	Lu, Ming 1,2; Park, Jang-Su 2
	2015-06-01
发表期刊	JOURNAL OF CELLULAR BIOCHEMISTRY
卷号	116 期号:6 页码:977-984
摘要	The expression of eukaryoticmolecular chaperones (heat shock proteins, HSPs) is triggered in response to a wide range of environmental stresses, including: heat shock, hydrogen peroxide, heavy metal, low-pH, or virus infection. Biochemical and genetic studies have clearly shown the fundamental roles of heat shock factor 1 (HSF1) in stress-inducible HSP gene expression, resistance to stress-induced cell death, carcinogenesis, and other biological phenomena. Previous studies show that acidic pH changes within the physiological range directly activate the HSF1 function in vitro. However, the detailed mechanism is unclear. Though computational pKa-predications of the amino acid side-chain, acidic-pH induced protonation of a histidine residue was found to be most-likely involved in this process. The histidine 83 (His83) residue, which could be protonated by mild decrease in pH, causes mild acidic-induced HSF1 activation (including in-vitro trimerization, DNA binding, in-vivo nuclear accumulation, and HSPs expression). His83, which is located in the loop region of the HSF1 DNA binding domain, was suggested to enhance the intermolecular force with Arginine 79, which helps HSF1 form a DNA-binding competent. Therefore, low-pH-induced activation of HSF1 by the protonation of histidine can help us better to understand the HSF1 mechanism and develop more therapeutic applications (particularly in cancer therapy). (C) 2015 Wiley Periodicals, Inc.
文章类型	Article
关键词	Heat Shock Factor 1 (Hsf1) Protonation Histidine Acidification
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
DOI	10.1002/jcb.25051
关键词[WOS]	SHOCK TRANSCRIPTION FACTOR ; DNA-BINDING DOMAIN ; HEAT-SHOCK ; INTRACELLULAR PH ; STRESS ; PROTEINS ; FACTOR-1 ; CANCER ; TRIMERIZATION ; METABOLISM
收录类别	SCI
语种	英语
WOS研究方向	Biochemistry & Molecular Biology ; Cell Biology
WOS类目	Biochemistry & Molecular Biology ; Cell Biology
WOS记录号	WOS:000352816400010
引用统计	被引频次：4[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qibebt.ac.cn/handle/337004/6733
专题	分子微生物工程研究组
作者单位	1.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Lab Biofuels, Qingdao 266061, Peoples R China 2.Pusan Natl Univ, Dept Chem, Pusan 609735, South Korea
推荐引用方式 GB/T 7714	Lu, Ming,Park, Jang-Su. Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification[J]. JOURNAL OF CELLULAR BIOCHEMISTRY,2015,116(6):977-984.
APA	Lu, Ming,&Park, Jang-Su.(2015).Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification.JOURNAL OF CELLULAR BIOCHEMISTRY,116(6),977-984.
MLA	Lu, Ming,et al."Protonation Behavior of Histidine during HSF1 Activation by Physiological Acidification".JOURNAL OF CELLULAR BIOCHEMISTRY 116.6(2015):977-984.